We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1.
- Authors
Leys, D; Tsapin, A S; Nealson, K H; Meyer, T E; Cusanovich, M A; Van Beeumen, J J
- Abstract
Fumarate respiration is one of the most widespread types of anaerobic respiration. The soluble fumarate reductase of Shewanella putrefaciens MR-1 is a periplasmic tetraheme flavocytochrome c. The crystal structures of the enzyme were solved to 2.9 A for the uncomplexed form and to 2.8 A and 2.5 A for the fumarate and the succinate-bound protein, respectively. The structures reveal a flexible capping domain linked to the FAD-binding domain. A catalytic mechanism for fumarate reduction based on the structure of the complexed protein is proposed. The mechanism for the reverse reaction is a model for the homologous succinate dehydrogenase (complex II) of the respiratory chain. In flavocytochrome c fumarate reductase, all redox centers are in van der Waals contact with one another, thus providing an efficient conduit of electrons from the hemes via the FAD to fumarate.
- Publication
Nature structural biology, 1999, Vol 6, Issue 12, p1113
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/70051